Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation
about
Aczonin, a 550-kD putative scaffolding protein of presynaptic active zones, shares homology regions with Rim and Bassoon and binds profilinStructural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.Differential remodeling of actin cytoskeleton architecture by profilin isoforms leads to distinct effects on cell migration and invasionPhosphorylation of profilin by ROCK1 regulates polyglutamine aggregationProfilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical propertiesA novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding siteCapping protein regulators fine-tune actin assembly dynamicsIncompatibility with Formin Cdc12p Prevents Human Profilin from Substituting for Fission Yeast Profilin: INSIGHTS FROM CRYSTAL STRUCTURES OF FISSION YEAST PROFILINRegulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering proteinPhosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actinThe characterization of ligand-specific maize (Zea mays) profilin mutantsAnalysis of the effects of polymorphism on pollen profilin structural functionality and the generation of conformational, T- and B-cell epitopesEVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 familySpecificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transductionCommon mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.The structure and function of proline recognition domains.Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylaseDiscovery of a Biological Mechanism of Active Transport through the Tympanic Membrane to the Middle Ear.Regulation and targeting of the fission yeast formin cdc12p in cytokinesis.Processive acceleration of actin barbed-end assembly by N-WASP.Ena/VASP Enabled is a highly processive actin polymerase tailored to self-assemble parallel-bundled F-actin networks with FascinFission yeast profilin is tailored to facilitate actin assembly by the cytokinesis formin Cdc12.EVH1 domains: structure, function and interactions.Characterization of profilin polymorphism in pollen with a focus on multifunctionality.Platelets and cancer: a casual or causal relationship: revisited.VASP is a processive actin polymerase that requires monomeric actin for barbed end association.A survey of left-handed polyproline II helicesPolyproline II structure in proteins: identification by chiroptical spectroscopies, stability, and functions.Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast.Parallel up-regulation of the profilin gene family following independent domestication of diploid and allopolyploid cotton (Gossypium).Determinants of Formin Homology 1 (FH1) domain function in actin filament elongation by formins.Nuclear Magnetic Resonance Structure of a Novel Globular Domain in RBM10 Containing OCRE, the Octamer Repeat Sequence MotifCaenorhabditis elegans expresses three functional profilins in a tissue-specific manner.The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.Model of formin-associated actin filament elongation.Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motilityReview of the mechanism of processive actin filament elongation by forminsHandedness preference and switching of peptide helices. Part I: Helices based on protein amino acids.Profilin1 biology and its mutation, actin(g) in disease.
P2860
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P2860
Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Structure of the profilin-poly ...... is and cytoskeletal regulation
@ast
Structure of the profilin-poly ...... is and cytoskeletal regulation
@en
Structure of the profilin-poly ...... is and cytoskeletal regulation
@nl
type
label
Structure of the profilin-poly ...... is and cytoskeletal regulation
@ast
Structure of the profilin-poly ...... is and cytoskeletal regulation
@en
Structure of the profilin-poly ...... is and cytoskeletal regulation
@nl
prefLabel
Structure of the profilin-poly ...... is and cytoskeletal regulation
@ast
Structure of the profilin-poly ...... is and cytoskeletal regulation
@en
Structure of the profilin-poly ...... is and cytoskeletal regulation
@nl
P2093
P2860
P356
P1476
Structure of the profilin-poly ...... is and cytoskeletal regulation
@en
P2093
P2860
P304
P356
10.1038/NSB1197-953
P577
1997-11-01T00:00:00Z